GP_BUNGE
ID GP_BUNGE Reviewed; 1437 AA.
AC P12430;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P04505};
DE Short=Gn;
DE AltName: Full=Glycoprotein G2;
DE Contains:
DE RecName: Full=Non-structural protein M {ECO:0000250|UniProtKB:P04505};
DE Short=NSm;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P04505};
DE Short=Gc;
DE AltName: Full=Glycoprotein G1;
DE Flags: Precursor;
GN Name=GP;
OS Bunyavirus germiston.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus.
OX NCBI_TaxID=11574;
OH NCBI_TaxID=53527; Culex.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3176688; DOI=10.1016/0168-1702(88)90068-8;
RA Pardigon N., Vialat P., Gerbaud S., Girard M., Bouloy M.;
RT "Nucleotide sequence of the M segment of Germiston virus: comparison of the
RT M gene product of several bunyaviruses.";
RL Virus Res. 11:73-85(1988).
CC -!- FUNCTION: Glycoprotein C and Glycoprotein N interact with each other
CC and are present at the surface of the virion. They are able to attach
CC the virion to a cell receptor and to promote fusion of membranes after
CC endocytosis of the virion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Glycoprotein C and Glycoprotein N interact with each other.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Glycoprotein C
CC alone is retained in the membrane of the endoplasmic reticulum, but not
CC transported to the Golgi. Coexpression of Glycoprotein C and
CC Glycoprotein N results in efficient transport of Glycoprotein C to the
CC Golgi complex, indicating that their interaction is essential for
CC proper targeting to this organelle, where virion budding occurs (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Glycoprotein N is retained in the Golgi complex
CC through a Golgi retention signal, which resides in the Glycoprotein N
CC transmembrane region. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein M]: Host Golgi apparatus
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
CC including nonstructural protein NSm, Glycoprotein C, and Glycoprotein
CC N.
CC -!- SIMILARITY: Belongs to the orthobunyavirus envelope glycoprotein
CC family. {ECO:0000305}.
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DR EMBL; M21951; AAA42778.1; -; Genomic_RNA.
DR PIR; S07430; S07430.
DR SMR; P12430; -.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host process; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR005167; Bunya_G1.
DR InterPro; IPR005168; Bunya_G2.
DR InterPro; IPR026400; Bunya_nonstruc_pro_NSm.
DR InterPro; IPR014413; M_poly_OrthobunV.
DR Pfam; PF03557; Bunya_G1; 1.
DR Pfam; PF03563; Bunya_G2; 1.
DR PIRSF; PIRSF003944; M_poly_OrthobunV; 1.
DR TIGRFAMs; TIGR04210; bunya_NSm; 1.
PE 3: Inferred from homology;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1437
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036786"
FT CHAIN 22..306
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036787"
FT CHAIN 307..481
FT /note="Non-structural protein M"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036788"
FT CHAIN 482..1437
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036789"
FT TOPO_DOM 22..207
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..373
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..1391
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1392..1412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1413..1437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 481..482
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1173
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1437 AA; 162494 MW; C4FB3001BD09A30D CRC64;
MAISTSLLIV ALLIKLCLVN TAPPISKCFQ DGILIAELKS SSGISEFCIK DDISILKSEI
TYSKNDTGIF MHSKVFRHWT VADWKQCNHT SAGGSTNVLE VDKNLNLVAK NYMCTRPCVI
TIDKENAQLL FQTEQLNQFE VTGTTISTGW FKSKTSVSLD NTCEHIKVTC GKKSLQFHAC
FKQHMSCVRF LHRSVLPGYM ASSICQNIEL IIIIILTLAI FIFMCIITRT YICYLMLPLF
APIAYLYGWL YNRSCKKCIC CGLAYHPFTN CGSYCVCGSR FETSDRMRLH RESGLCQGFK
SLRVARSLCK SKGSSLVISI LTAMLILSFI TPLEAMTTNY PDDKKFTLKE VNDIVLGRDM
EQELKSSILI LMSICGIGII LIFFGLTVLL EIVLELIAKR STIFCKECNL IHDKKSMTYR
GDFTNKCGFC PCGELEDPEG LVIHTTRKSC TYYIKIRNLK LIMLIFSIVI LMQNATMLVV
AGENCWTNTE IKADCVGPLI GPSACTNKGS KTYKTVAQEL VTASKITQLD ADKYVLLGDT
IESALDAITS QKHYSAMHLL ETMFLMKHCD YYKVYEHNSG YSQTKWRLIA IANSFDICTN
TPTPNFCKCL SDSSCSTTTL NFATSMNATY TSKVEFFNHD FTLFLDIFEA AFPGSATAFL
FKKIKEKNPY QAFEMMGKIA NKYPNNKLLV VILKYGQYMV GLSHASTYQL KQEWVAKSLS
LTRAQRTGLK MSMANAEPGP ATKECSDAKT IACLTPKFQV EVNNLMSCGA SPNFKIYVKT
GELYKAHDRN SVWCLNDMHC LTPYTPANAE IITTMKKMDC WQDNPKQPTD EYAIPKRSCQ
MKDRGLCNSG ADKWKIIKCD NHKLFYTDAL ERRDPASIVG SNHCFSEKCQ IERYPINPTS
LTNCEWLYRA VRPEYIKKLS LQTIEEYKKA IADKLTHTLQ LYHFAPLLEN LPHIKPTYKY
ITAQGTYTAD GIEGASITTS IPALSGTSVG FKINAKDGTD LLDIVVYIKA SVVKSIYNHI
YDTGPTININ SKHDELCTGQ CPKKIPADPN WLTFSQERTS RWGCEEFGCL AINTGCVYGS
CQDVIRTETK VYRKANEETV MLTVCITYPG HTFCTDVNAH EPKITDELEL QFKTIDIKSL
PNLVAVTNHK LYTGQINDLG TFGQMCGNVQ KTNTSHTGAG TPKFDYTCYS ASRKDIIIRR
CYNNNYDSCR LLNQESDLLF DDNHETLVVY NNKRLNGELA LKLLLGDIQY KLYTENMELE
LEAKCVGCVG CFESYQCNLQ ITSSLDETAL YLVPVSHFHD RIQIKTTKKD YAMKISCTRD
PGDKASFRVC GKSYDFNFHT VPKNDKIEVN VGDETSYIKE KDNRCGRWLC RVRDEGLSVI
FEPLNNFFGN YLNMFLYILG GIILLFLALY ILMPMCARLR DELKRNERLH QMEMKKR
